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Cdc25 is a dual specificity phosphatase with three isoforms in mammalian cells - Cdc25A, B and C. Cdc25 activates cdk complexes that drive the cell cycle. Cdc25 is involved in the DNA damage checkpoints and is known as a key mediator of cell cycle progression.
|Cat No||Product Name / Activity|
|Potent, selective Cdc25 phosphatase inhibitor|
|Selective Cdc25 dual specificity phosphatase inhibitor|
Cdc25 is a dual specificity phosphatase with three isoforms in mammalian cells - Cdc25A, B and C. Cdc25 activates cdk complexes that control progression through the cell cycle. Cdc25 is also involved in the DNA damage checkpoints.
Regulation of Cdc25 occurs through a variety of mechanisms including phosphorylation, interaction with 14.3.3 proteins, subcellular localization and protein degradation. Cdc25B is phosphorylated and activated by aurora kinase A at the start of mitosis, and as mitosis progresses is then further phosphorylated in an auto-amplification loop, along with Cdc25C, by the CDK1/cyclin B complex. Cdc25C is also phosphorylated during mitosis by PLK1, leading to greater activity of the CDK1/cyclin B complex. Similarly, Cdc25A acts during the G1/S phase of the cell cycle in concert with the CDK2/cyclin E complex. Both Cdc25A and Cdc25B can be activated by the DNA damage checkpoint kinase, Chk1 and thereby inhibit mitosis.
Cdc25 is a key mediator of cell cycle progression. Consequently, there is a strong link between Cdc25 and cancer. Expression of Cdc25A and Cdc25B is upregulated in certain cancer types, frequently those with more aggressive tumors and poor prognosis; the development of specific Cdc25 inhibitors is therefore of great therapeutic interest.
In normal cells, each stage of the cell cycle is tightly regulated, however in cancer cells many genes and proteins that are involved in the regulation of the cell cycle are mutated or over expressed. Adapted from the 2015 Cancer Product Guide, Edition 3, this poster summarizes the stages of the cell cycle and DNA repair. It also highlights strategies for enhancing replicative stress in cancer cells to force mitotic catastrophe and cell death.
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